ID A0A6A3B838_HIBSY Unreviewed; 1455 AA.
AC A0A6A3B838;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 02-APR-2025, entry version 14.
DE SubName: Full=Pectin lyase-like superfamily protein isoform 1 {ECO:0000313|EMBL:KAE8711987.1};
GN ORFNames=F3Y22_tig00110266pilonHSYRG00067
GN {ECO:0000313|EMBL:KAE8711987.1};
OS Hibiscus syriacus (Rose of Sharon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8711987.1, ECO:0000313|Proteomes:UP000436088};
RN [1] {ECO:0000313|EMBL:KAE8711987.1, ECO:0000313|Proteomes:UP000436088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAE8711987.1};
RA Kim Y.-M.;
RT "Draft genome information of white flower Hibiscus syriacus.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SPT5 family.
CC {ECO:0000256|ARBA:ARBA00006956}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAE8711987.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VEPZ02000903; KAE8711987.1; -; Genomic_DNA.
DR Proteomes; UP000436088; Unassembled WGS sequence.
DR GO; GO:0032044; C:DSIF complex; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
DR GO; GO:0032784; P:regulation of DNA-templated transcription elongation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:TreeGrafter.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR FunFam; 2.30.30.30:FF:000053; Protein RNA-directed DNA methylation 3; 1.
DR FunFam; 3.30.70.940:FF:000016; Uncharacterized protein; 1.
DR Gene3D; 2.30.30.30; -; 2.
DR Gene3D; 3.30.70.940; NusG, N-terminal domain; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125:SF8; PROTEIN RNA-DIRECTED DNA METHYLATION 3; 1.
DR PANTHER; PTHR11125; SUPPRESSOR OF TY 5; 1.
DR Pfam; PF23042; KOW1_SPT5; 1.
DR Pfam; PF23291; KOW4_SPT5; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR SMART; SM00739; KOW; 3.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KAE8711987.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000436088};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 289..316
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 509..536
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 618..645
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..598
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1199
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1238
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1401
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1445
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1455
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1455 AA; 156193 MW; 05821EF2B818CBDF CRC64;
MSSKGKEKEV VYGKRKVSAG RSGGVTEESR RKRRNRGVLQ FFEDSAEDDG SDASDGSDIN
DCKADLINVF FVLFGVFYVS FWSVALYDCL FLRLLGFTPF DFVLHFGFKG FRLWRCLTFS
RQNDVLQEEP DLDVNKNPWK AHNVPFVPKE EVIEEEFDKM MEERYRGGAR FTTFEEDYEA
KGSIDKNSTV PPAKDPVIWK VKCVVGRERH SAFCLMQKFI DMKSLGTKLQ IISAFSVDHV
KGFFFIEADK QCDINEACKG LTYIYSSRLA PVPSNEVYHL LNVRTKCCEI SKGMWARIKN
GKYKGDLAQV VAVNNEKKKA TVKLIPRIDL QAMAAKFGSG VSISRTVIPA PKLISLIELE
EFRPLIQFRR DRDTSIGFQV LDGMMLKDGY LYKKVSIDSL SCWGIMPTEE ELLKFSNSDN
NESDDLEWLS QLYAVTTYQQ LVNNLFHVLF HLHCSRKDFG LIVGMEKDDR YKILREAPEG
PIVVTVEKHE LKNGPLDTKF TALDKHSKTI SINDTVKVLE GQYEGKQGTV KQIYRGTIFL
YDENETDNGG FFCCKSPMCE KIKQRSDKCS EKGGDPGGTS DYGDFVSSPK SPISPEKPWQ
SQEKETKSDF NRGNIDGMFS IGQTLRIRVG PLKGYLCRVL AVYRSDVTVK VGSKQKVLKV
KNEHLAEVQG KSTAANTNEH DGSTSFKPFG SEASTGDWLN GAGTSAEGGG WNAERCSLSL
YVLDGEGSAW DTKPTANQNS SWGAAAPSGD NDNKTDGASS AWENNTSTQQ NSAWATGGSD
HNSNRGSWNN SAPKIDSGGG ASDAWVKTIT GGGPSGASQD VDNDGWDKGK GVAEEGSWGK
NKKSSVNEGN WNNNDVGSNQ QGSWGIKNDA SVGQDNSWGN TAEKWNNKDG IGGSKGNWGS
SKPSAEDAKG SWGKQDGGSS LNQSDGWNKE KAADVGTSGG KQDGGSSWYK QLGGSSWGVS
NTKSGGGAIQ DAGQDSGWSK RSSWNSGSGG TNQEPGWAKK NDSDFGSGDA TKDSTWGKKS
DWNSGSADAN QESKKNSWGS GTTDAGPDSG WGQRGSWNSG SGNANQNPGW TKKSDSGFAA
GDATNDSSWE KKGAADASRD SNWGKKSSWG TGTDSGQDAG WGKKGGWNPG SSSAGEDSGW
KSKSKWNSGA GDANQDSGWK PKNDWKSGSG NEDQNEPFSG RGGGSWRGGF GGRDGSGRGF
RGRGDSDGGG FRGRGRSDRG RGRSDRGGFG GDGGGYGGRG DRGGDRGGYG GRGGDRGGYR
GRGGDRGGYG GRGRGRRDEN GGWNNGGDSG ENKSYGWNKE GNQGWNGGGA KTCGQSNADN
RGQSSGWSQP GGWNKGTGST NEAGGNQDTS WKSSNSSDGN KWSGWNQSTC SKDVKESTSQ
GHGWEKSSAT AAGGGWGGRG SGSAEQVEPK TADEGASSGW NKPKDGEGSS GNQDAWGKAS
SSSWGQGSGS RKGGW
//